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      Protein structure

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      https://www.riss.kr/link?id=M341969

      • 저자
      • 발행사항

        Oxford ; New York : IRL Press at Oxford University Press, c1993

      • 발행연도

        1993

      • 작성언어

        영어

      • 주제어
      • DDC

        574.19/245 판사항(20)

      • ISBN

        019963310X (pbk.) :

      • 자료형태

        단행본(다권본)

      • 발행국(도시)

        England

      • 서명/저자사항

        Protein structure / N.J. Darby and T.E. Creighton.

      • 형태사항

        xiii, 99 p. : ill. (some col.) ; 23 cm.

      • 총서사항

        In focus In focus (Oxford, England)

      • 일반주기명

        Includes bibliographical references and index.

      • 소장기관
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        • 이화여자대학교 도서관 소장기관정보 Deep Link
        • 인천대학교 학산도서관 소장기관정보
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      목차 (Table of Contents)

      • CONTENTS
      • Abbreviations = xi
      • Abbreviations for amino acids = xiii
      • 1. Basic aspects of polypeptide structure
      • The covalent structures of proteins = 1
      • CONTENTS
      • Abbreviations = xi
      • Abbreviations for amino acids = xiii
      • 1. Basic aspects of polypeptide structure
      • The covalent structures of proteins = 1
      • Non-covaient forces in protein structure = 3
      • Electrostatic interactions = 3
      • van der Waals interactions = 5
      • Hydrogen bonds = 5
      • Hydrophobic interactions = 5
      • The amino acid residues = 7
      • Primary structures of proteins = 8
      • Three-dimensional aspects of polypeptide structure = 9
      • Conformations of polypeptides = 9
      • Regular polypeptide structures = 13
      • The structures of fibrous proteins = 16
      • Silk fibroin = 16
      • Collagen = 18
      • Coiled-coils = 18
      • Further reading = 21
      • References = 21
      • 2. The three-dimensional structures of proteins
      • Introduction = 23
      • Determining protein structure = 23
      • CD spectroscopy = 23
      • X-ray diffraction = 24
      • NMR spectroscopy = 25
      • Structural organization in globular proteins = 26
      • Tertiary structure = 26
      • Protein interiors and exteriors = 26
      • Secondary structure = 27
      • Loops and turns = 28
      • Disulphide bonds = 28
      • Domains = 28
      • Supersecondary structure and folding patterns = 30
      • Quaternary structure = 35
      • Flexibility in protein structures = 37
      • Evolutionarily related proteins = 38
      • Predicting protein structure = 39
      • Protein design = 40
      • Further reading = 41
      • References = 41
      • 3. Proteins in solution and in membranes
      • Introduction = 43
      • Proteins in aqueous solution = 43
      • Aqueous solubility = 43
      • Ionization = 44
      • Membrane proteins = 45
      • Stability of the folded state = 47
      • Unfolding = 47
      • The thermodynamics of unfolding = 50
      • Rationalizing protein stability = 51
      • Other factors that affect protein stability = 54
      • Protein folding = 55
      • General characteristics of protein folding = 55
      • Identifying folding intermediates = 56
      • Biosynthetic folding = 58
      • Further reading = 59
      • References = 60
      • 4. Ligand binding and protein function
      • Introduction = 63
      • Ligand binding = 63
      • Studying protein―ligand interactions = 63
      • General properties of protein―ligand interactions = 64
      • The relationship between protein structure and ligand binding = 65
      • Calcium-binding proteins = 66
      • Redox proteins = 67
      • Nucleotide-binding proteins = 69
      • DNA-binding proteins = 71
      • Helix―turn―helix proteins = 73
      • Zinc-containing DNA recognition elements = 73
      • Other DNA-binding motifs = 76
      • Regulation of ligand binding = 79
      • Allosteric regulation = 79
      • Reversible covalent modification = 83
      • Further reading = 88
      • References = 89
      • Glossary = 91
      • Index = 95
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